Identification and Characterization of the Haloperoxidase VPO-RR from Rhodoplanes roseus by Genome Mining and Structure-Based Catalytic Site Mapping

Halogenating enzymes have evolved in considerable mechanistic diversity. The apparent need for secondary metabolism coincides with the current to introduce halogens synthetic products. potential of halogenating and, especially, vanadate-dependent haloperoxidases has been insufficiently exploited purposes. In this work, we identified halogenase sequences by screening algal, fungal, and protobacterial sequence databases, structural modeling putative halogenases, mapping comparing active sites. a final step, individual were expressed kinetically characterized. A haloperoxidase from Rhodoplanes roseus was heterologously expressible E. coli could be purified homogeneity. kinetic data revealed higher turnover number than known VClPO-CI no inhibitory effect bromide, rendering enzyme promising biocatalyst. Other predicted not successfully yet but these present wide taxonomic variety.